Title : Chibby forms a homodimer through a heptad repeat of leucine residues in its C-terminal coiled-coil motif.

Pub. Date : 2009 May 12

PMID : 19435523






7 Functional Relationships(s)
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Protein Name
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1 Chibby forms a homodimer through a heptad repeat of leucine residues in its C-terminal coiled-coil motif. Leucine chibby family member 1, beta catenin antagonist Homo sapiens
2 Alanine substitutions of two or more of four critical leucine residues within the C-terminal heptad repeats completely eliminate the Cby-Cby interaction. Alanine chibby family member 1, beta catenin antagonist Homo sapiens
3 Alanine substitutions of two or more of four critical leucine residues within the C-terminal heptad repeats completely eliminate the Cby-Cby interaction. Alanine chibby family member 1, beta catenin antagonist Homo sapiens
4 Alanine substitutions of two or more of four critical leucine residues within the C-terminal heptad repeats completely eliminate the Cby-Cby interaction. Leucine chibby family member 1, beta catenin antagonist Homo sapiens
5 Alanine substitutions of two or more of four critical leucine residues within the C-terminal heptad repeats completely eliminate the Cby-Cby interaction. Leucine chibby family member 1, beta catenin antagonist Homo sapiens
6 CONCLUSION: Our comprehensive mutational analysis of the Cby coiled-coil domain reveals that the four heptad leucine residues play an essential role in mediating Cby homodimerization. Leucine chibby family member 1, beta catenin antagonist Homo sapiens
7 CONCLUSION: Our comprehensive mutational analysis of the Cby coiled-coil domain reveals that the four heptad leucine residues play an essential role in mediating Cby homodimerization. Leucine chibby family member 1, beta catenin antagonist Homo sapiens